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InterPro: IPR015892 Carbonic anhydrase, prokaryotic-like, conserved site

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UniProtKB

Matches:

1428 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR015892 Carbonic_anhydrase_CS

Secondary

IPR001765

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00704	PROK_CO2_ANHYDRASE_1	1143
PROSITE pattern	PS00705	PROK_CO2_ANHYDRASE_2	1172
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001765 Carbonic anhydrase

GO Term annotation Help

Process

GO:0015976 carbon utilization

Function

GO:0004089 carbonate dehydratase activity
GO:0008270 zinc ion binding

InterPro annotation

Entry Details in BioMart

Abstract

Carbonic anhydrases (EC:4.2.1.1) (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate [1]. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation [2]. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's (see IPR001148). Hypothetical proteins yadF from Escherichia coli and HI1301 from Haemophilus influenzae also belong to this family.

Structural links Help

PDB - click here

SCOP: c.53.2.1

CATH: 3.40.1050.10

Database links Help

PDBe-motif: PS00704 , PS00705

Enzyme: EC:4.2.1.1

PROSITE doc: PDOC00586

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR015892

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P27140 Carbonic anhydrase, chloroplastic

P45148 Carbonic anhydrase 2

P53615 Carbonic anhydrase

Q54735 Carbonic anhydrase

Q5BCC5 Carbonic anhydrase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001765	Carbonic anhydrase
IPR015892	Carbonic anhydrase, prokaryotic-like, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Guilloton MB, Korte JJ, Lamblin AF, Fuchs JA, Anderson PM. Carbonic anhydrase in Escherichia coli. A product of the cyn operon. J. Biol. Chem. 267 3731-4 1992 [PubMed: 1740425] http://intl.jbc.org/cgi/content/abstract/267/6/3731
2.	Fukuzawa H, Suzuki E, Komukai Y, Miyachi S. A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942. Proc. Natl. Acad. Sci. U.S.A. 89 4437-41 1992 [PubMed: 1584776] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1584776&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Mitsuhashi S, Mizushima T, Yamashita E, Yamamoto M, Kumasaka T, Moriyama H, Ueki T, Miyachi S, Tsukihara T. X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration. J. Biol. Chem. 275 2000 5521-6 [PubMed: 10681531] http://dx.doi.org/10.1074/jbc.275.8.5521
	Kimber MS, Pai EF. The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases. EMBO J. 19 2000 1407-18 [PubMed: 10747009] http://dx.doi.org/10.1093/emboj/19.7.1407
	Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY. Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity. Protein Sci. 10 2001 911-22 [PubMed: 11316870] http://dx.doi.org/10.1110/ps.46301
	Cronk JD, Rowlett RS, Zhang KY, Tu C, Endrizzi JA, Lee J, Gareiss PC, Preiss JR. Identification of a novel noncatalytic bicarbonate binding site in eubacterial beta-carbonic anhydrase. Biochemistry 45 2006 4351-61 [PubMed: 16584170] http://dx.doi.org/10.1021/bi052272q

InterPro 23.1